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Reviewed, UniProtKB/Swiss-Prot O49432 (QRT3_ARATH)

Last modified February 9, 2010. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Polygalacturonase QRT3
      Short name=PG QRT3
      Short name=AtQRT3
    EC=3.2.1.15
Alternative name(s):
    Protein QUARTET 3
    Pectinase QRT3
Gene names
Name: QRT3
Ordered Locus Names: At4g20050
ORF Names: F18F4.150
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Polygalacturonase required for degrading the pollen mother cell wall during microspore development. Ref.1

Catalytic activity

Random hydrolysis of (1->4)-alpha-D-galactosiduronic linkages in pectate and other galacturonans.

Subcellular location

Secretedcell wall Ref.1.

Tissue specificity

Expressed in the tapetum cells in the anthers and in the ovules of open flowers. Ref.1

Developmental stage

Transiently expressed during the early microspore stage. Ref.1

Disruption phenotype

The mature pollen grains are arranged in a tetrad. A layer of material is frequently deposited on the surface of the distal region of the pollen grains. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 28 family.

Contains 3 PbH1 repeats.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell wall
Secreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

microsporogenesis Ref.1

Inferred from mutant phenotype. Source: TAIR

   Cellular componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionpolygalacturonase activity Ref.1

Inferred from direct assay. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 481454Polygalacturonase QRT3
PRO_0000370639

Regions

Repeat203 – 22624PbH1 1
Repeat261 – 28222PbH1 2
Repeat356 – 37722PbH1 3

Amino acid modifications

Glycosylation4151N-linked (GlcNAc...) Potential
Glycosylation4551N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O49432-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 9299F16297364257

FASTA48151,659
        10         20         30         40         50         60 
MELRKSQVAM PVFLAIMSLM VSQVVFAEKD SGSMSPHDRA LAEMQALKAS LVRRNLPALV 

        70         80         90        100        110        120 
SPPPTPPQAV PGPRVYQVIS YGADPTGKLD STDAILKAME EAFDGPNHGV LMQGINDLGG 

       130        140        150        160        170        180 
ARIDLQGGSY LISRPLRFPS AGAGNLLISG GTLRASNDFP VDRYLIELKD ESSKLQYIFE 

       190        200        210        220        230        240 
YITLRDLLID CNYRGGAIAV INSLRTSIDN CYITRFGDTN GILVKSGHET YIRNSFLGQH 

       250        260        270        280        290        300 
ITAGGDRGER SFSGTAINLM GNDNAVTDTV IFSARIGVMV SGQANLLSGV HCYNKATGFG 

       310        320        330        340        350        360 
GTGIYLRLPG LTQNRIVNSY LDYTGIVAED PVQLQISGTF FLGDAFILLK SIAGYIRGVS 

       370        380        390        400        410        420 
IVDNMFSGSG HGVQIVQLDQ RNTAFDDVGQ VVVDRNSVNG MVEKSTVARG SVDGNGTSWT 

       430        440        450        460        470        480 
VDFNPVLLFP DLINHVQYTL VASEAGVFPL HALRNVSDNR VVVETNAPVT GTVYVTVNQG 


V 

« Hide

References

« Hide 'large scale' references
[1]"Microspore separation in the quartet 3 mutants of Arabidopsis is impaired by a defect in a developmentally regulated polygalacturonase required for pollen mother cell wall degradation."
Rhee S.Y., Osborne E., Poindexter P.D., Somerville C.R.
Plant Physiol. 133:1170-1180(2003) [PubMed: 14551328] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
Strain: cv. Columbia and cv. Landsberg erecta.
[2]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY268942 mRNA. Translation: AAQ83300.1.
AY268941 Genomic DNA. Translation: AAQ83299.1.
AL021637 Genomic DNA. Translation: CAA16613.1.
AL161552 Genomic DNA. Translation: CAB79005.1.
IPIIPI00548352.
PIRT04889.
RefSeqNP_001078410.1.
NP_193738.1.
UniGeneAt.32754

3D structure databases

SMRO49432. Positions 76-236.
ModBaseSearch...

Proteomic databases

PRIDEO49432.

Genome annotation databases

GeneID827750.
GenomeReviewsGene locus AT4G20050 in contig CT486007_GR.
KEGGath:AT4G20050.
NMPDRfig|3702.1.peg.19835.

Organism-specific databases

TAIRAt4g20050.

Phylogenomic databases

HOGENOMHBG318504.
InParanoidO49432.
OMAGNDNSVS.

Gene expression databases

ArrayExpressO49432.
GenevestigatorO49432.

Family and domain databases

InterProIPR006626. PbH1.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SMARTSM00710. PbH1. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQRT3_ARATH
AccessionPrimary (citable) accession number: O49432
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: June 1, 1998
Last modified: February 9, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents